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Ammonium transporter Rh type B (Rhesus blood group family type B glycoprotein) (Rh family type B glycoprotein) (Rh type B glycoprotein)

 RHBG_MOUSE              Reviewed;         455 AA.
Q8BUX5; Q9QXP1;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-MAR-2018, entry version 110.
RecName: Full=Ammonium transporter Rh type B;
AltName: Full=Rhesus blood group family type B glycoprotein;
Short=Rh family type B glycoprotein;
Short=Rh type B glycoprotein;
Name=Rhbg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
AND GLYCOSYLATION.
TISSUE=Liver;
PubMed=11024028; DOI=10.1074/jbc.M007528200;
Liu Z., Peng J., Mo R., Hui C.-C., Huang C.-H.;
"Rh type B glycoprotein is a new member of the Rh superfamily and a
putative ammonia transporter in mammals.";
J. Biol. Chem. 276:1424-1433(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=C3H/HeJ; TISSUE=Kidney cortex;
PubMed=15353405; DOI=10.1152/ajprenal.00419.2003;
Nakhoul N.L., Dejong H., Abdulnour-Nakhoul S.M., Boulpaep E.L.,
Hering-Smith K., Hamm L.L.;
"Characteristics of renal Rhbg as an NH4(+) transporter.";
Am. J. Physiol. 288:F170-F181(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12388412; DOI=10.1152/ajprenal.00050.2002;
Verlander J.W., Miller R.T., Frank A.E., Royaux I.E., Kim Y.-H.,
Weiner I.D.;
"Localization of the ammonium transporter proteins RhBG and RhCG in
mouse kidney.";
Am. J. Physiol. 284:F323-F337(2003).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12730882; DOI=10.1016/S0016-5085(03)00277-4;
Weiner I.D., Miller R.T., Verlander J.W.;
"Localization of the ammonium transporters, Rh B glycoprotein and Rh C
glycoprotein, in the mouse liver.";
Gastroenterology 124:1432-1440(2003).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15576624; DOI=10.1152/ajpgi.00418.2004;
Handlogten M.E., Hong S.-P., Zhang L., Vander A.W., Steinbaum M.L.,
Campbell-Thompson M., Weiner I.D.;
"Expression of the ammonia transporter proteins Rh B glycoprotein and
Rh C glycoprotein in the intestinal tract.";
Am. J. Physiol. 288:G1036-G1047(2005).
[8]
FUNCTION.
PubMed=16131648; DOI=10.1152/ajprenal.00147.2005;
Mak D.-O., Dang B., Weiner I.D., Foskett J.K., Westhoff C.M.;
"Characterization of ammonia transport by the kidney Rh glycoproteins
RhBG and RhCG.";
Am. J. Physiol. 290:F297-F305(2006).
-!- FUNCTION: Functions as a specific ammonium transporter.
{ECO:0000269|PubMed:15353405, ECO:0000269|PubMed:16131648}.
-!- SUBUNIT: Interacts (via C-terminus) with ANK2 and ANK3; required
for targeting to the basolateral membrane. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
membrane protein. Cytoplasmic vesicle membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in kidney by connecting segments and
collecting tubules. Also expressed in liver by perivenous
hepatocytes. Expressed in the forestomach and the fundus of the
stomach. Expressed in duodenum, jejunum, ileum and colon at the
level of villous (at protein level). Specifically expressed in
kidney where it is restricted to the epithelial linings of the
convoluted tubules and the loop of Henle. Also detected in ovary.
Expressed by hepatocytes and dermal hair follicles and papillae.
{ECO:0000269|PubMed:11024028, ECO:0000269|PubMed:12388412,
ECO:0000269|PubMed:12730882, ECO:0000269|PubMed:15576624}.
-!- DEVELOPMENTAL STAGE: Detected in embryos at E15 and E17. Expressed
in kidney, skin and liver of E16.5 embryos.
{ECO:0000269|PubMed:11024028}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11024028}.
-!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49)
family. Rh subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF193808; AAF19371.1; -; mRNA.
EMBL; AY254685; AAP81167.1; -; mRNA.
EMBL; AK081882; BAC38359.1; -; mRNA.
EMBL; BC029236; AAH29236.1; -; mRNA.
CCDS; CCDS17466.1; -.
RefSeq; NP_067350.2; NM_021375.3.
UniGene; Mm.103777; -.
ProteinModelPortal; Q8BUX5; -.
STRING; 10090.ENSMUSP00000130767; -.
iPTMnet; Q8BUX5; -.
PhosphoSitePlus; Q8BUX5; -.
MaxQB; Q8BUX5; -.
PaxDb; Q8BUX5; -.
PRIDE; Q8BUX5; -.
Ensembl; ENSMUST00000171887; ENSMUSP00000130767; ENSMUSG00000104445.
GeneID; 58176; -.
KEGG; mmu:58176; -.
UCSC; uc008pui.1; mouse.
CTD; 57127; -.
MGI; MGI:1927379; Rhbg.
eggNOG; KOG3796; Eukaryota.
eggNOG; ENOG410XTF8; LUCA.
GeneTree; ENSGT00390000005787; -.
HOGENOM; HOG000007656; -.
HOVERGEN; HBG004374; -.
InParanoid; Q8BUX5; -.
KO; K06580; -.
OMA; DSQCYED; -.
OrthoDB; EOG091G06KX; -.
PhylomeDB; Q8BUX5; -.
TreeFam; TF314450; -.
Reactome; R-MMU-444411; Rhesus glycoproteins mediate ammonium transport.
ChiTaRS; Rhbg; mouse.
PRO; PR:Q8BUX5; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000104445; -.
CleanEx; MM_RHBG; -.
Genevisible; Q8BUX5; MM.
GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:UniProtKB.
GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0030506; F:ankyrin binding; ISO:MGI.
GO; GO:0015696; P:ammonium transport; IDA:UniProtKB.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
GO; GO:0070634; P:transepithelial ammonium transport; ISO:MGI.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
InterPro; IPR002229; RhesusRHD.
Pfam; PF00909; Ammonium_transp; 1.
PRINTS; PR00342; RHESUSRHD.
1: Evidence at protein level;
Ammonia transport; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 455 Ammonium transporter Rh type B.
/FTId=PRO_0000283599.
TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.
TRANSMEM 11 31 Helical. {ECO:0000255}.
TOPO_DOM 32 58 Extracellular. {ECO:0000255}.
TRANSMEM 59 79 Helical. {ECO:0000255}.
TOPO_DOM 80 83 Cytoplasmic. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TOPO_DOM 105 121 Extracellular. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 146 Cytoplasmic. {ECO:0000255}.
TRANSMEM 147 167 Helical. {ECO:0000255}.
TOPO_DOM 168 175 Extracellular. {ECO:0000255}.
TRANSMEM 176 198 Helical. {ECO:0000255}.
TOPO_DOM 199 216 Cytoplasmic. {ECO:0000255}.
TRANSMEM 217 237 Helical. {ECO:0000255}.
TOPO_DOM 238 248 Extracellular. {ECO:0000255}.
TRANSMEM 249 269 Helical. {ECO:0000255}.
TOPO_DOM 270 279 Cytoplasmic. {ECO:0000255}.
TRANSMEM 280 300 Helical. {ECO:0000255}.
TOPO_DOM 301 301 Extracellular. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 343 Cytoplasmic. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TOPO_DOM 365 390 Extracellular. {ECO:0000255}.
TRANSMEM 391 411 Helical. {ECO:0000255}.
TOPO_DOM 412 455 Cytoplasmic. {ECO:0000255}.
REGION 413 421 Interaction with ANK3. {ECO:0000250}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 195 195 W -> R (in Ref. 1; AAF19371 and 4;
AAH29236). {ECO:0000305}.
SEQUENCE 455 AA; 49543 MW; C8D57B88A37089D2 CRC64;
MARVPRHRRL VLPLLCLLFQ GATALLFAIF VRYNHETDAA LWHWGNHSNV DNEFYFRYPS
FQDVHVMVFV GFGFLMVFLQ RYGFSSVGFT FLVASLTLQW ATLLQGFLHS FHGGHIHVGV
ESLINADFCA GAVLISFGAV LGKTGPAQLL LMALLEAVLF SVNEFILLSL LGVRDAGGSM
TIHTFGAYFG LFLSWVLYRS QLEKSRHRQS SVYNSDLFAM IGTIFLWVFW PSFNSAPTAL
GDGQHRTVVN TYYSLTASTL STFALSALVS GDGRLDMVHV QNAALAGGVV VGTSSEMMLT
PFGALAAGFL AGTVSTLGYK FFTPILESRF KLQDTCGVHN LHGMPGVLGA ILGVVVAALA
THEAYGDGLQ SVFPLIAKGQ RSATSQAVYQ LFGMFVTLVF ASVGGSLGGL LLRLPFLDSP
PDSQCFEDQV YWEVPGEQET ETQRPLRGGE SDTRA


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